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dc.contributor.authorKazmierski, Michelle Nicole
dc.date.accessioned2014-03-03T20:20:39Z
dc.date.available2014-03-03T20:20:39Z
dc.date.issued2002-12
dc.identifier.otherkazmierski_michelle_n_200212_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/kazmierski_michelle_n_200212_ms
dc.identifier.urihttp://hdl.handle.net/10724/20598
dc.description.abstractDespite its widespread utilization, information relating to the characterization of commercially available whey protein isolate (WPI) is limited. Further insight into its behavior in mixed systems can enhance its use as a “value-added” ingredient. The thermal aggregation behavior of WPI was examined, as well as interactions between -lactoglobulin, the main functional protein in whey, with a high methoxyl and a pectinesterase-modified pectin at low pH, and stability of orange juice with added whey protein. Molecular weight averages and distribution of WPI aggregates varied significantly with temperature and concentration. Upon heating 10% WPI solutions, native protein decreased with increasing temperature and hydrodynamic diameters increased with temperature. Protein composition of the aggregates did not change upon heating. Pectin charge distribution affected the formation of soluble complexes with -lactoglobulin. Fortification was most stable upon addition of -lactoglobulin and WPI at pH 3.0 and a heat treatment of 85°C.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectWhey protein isolate
dc.subjectHeat-induced aggregation,
dc.titleThermally induced aggregation of whey proteins : characterization of protein isolates and beta-lactoglobulin/ pectin interactions
dc.typeThesis
dc.description.degreeMS
dc.description.departmentFood Science and Technology
dc.description.majorFood Science
dc.description.advisorMilena Corredig
dc.description.committeeMilena Corredig
dc.description.committeeLouise Wicker
dc.description.committeeRobert Shewfelt


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